Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Andrew M. Powl"'
Autor:
Nazzareno D’Avanzo, Andrew J. Miles, Andrew M. Powl, Colin G. Nichols, B.A. Wallace, Andrias O. O’Reilly
Cytoplasmic domains frequently promote functional assembly of multimeric ion channels. To investigate structural determinants of this process, we generated the ‘T1-chimera’ construct of the NaChBac sodium channel by truncating the C-terminal doma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fc8b2d072f6f972ab0f8f04984a2bc4
https://eprints.bbk.ac.uk/id/eprint/47007/8/47007a.pdf
https://eprints.bbk.ac.uk/id/eprint/47007/8/47007a.pdf
Autor:
Shimul Chandra Saha, Alexander J Henderson, Andrew M Powl, B A Wallace, Maurits R R de Planque, Hywel Morgan
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0131286 (2015)
This paper describes the use of a newly-developed micro-chip bilayer platform to examine the electrophysiological properties of the prokaryotic voltage-gated sodium channel pore (Na(v)Sp) from Silicibacter pomeroyi. The platform allows up to 6 bilaye
Externí odkaz:
https://doaj.org/article/e797db9effe94d4d88f774b1fad0c900
Autor:
Nazzareno D'Avanzo, Emily C McCusker, Andrew M Powl, Andrew J Miles, Colin G Nichols, B A Wallace
Publikováno v:
PLoS ONE, Vol 8, Iss 4, p e61216 (2013)
The lipid bilayer is important for maintaining the integrity of cellular compartments and plays a vital role in providing the hydrophobic and charged interactions necessary for membrane protein structure, conformational flexibility and function. To d
Externí odkaz:
https://doaj.org/article/c7a1618d6fb14c50a604b18925695d3e
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1818:889-895
The thermal stabilities of the extramembranous and transmembranous regions of the bacterial voltage-gated sodium channel NaChBac have been characterised using thermal-melt synchrotron radiation circular dichroism (SRCD) spectroscopy. A series of cons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30f79bf263e2bddebbae39c9f626890d
https://doi.org/10.1016/j.bbamem.2011.12.019
https://doi.org/10.1016/j.bbamem.2011.12.019
Publikováno v:
Proceedings of the National Academy of Sciences. 107:14064-14069
Extramembranous domains play important roles in the structure and function of membrane proteins, contributing to protein stability, forming association domains, and binding ancillary subunits and ligands. However, these domains are generally flexible
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c4c43c8c01b3c46b83fe04b70a983c9
https://doi.org/10.1073/pnas.1001793107
https://doi.org/10.1073/pnas.1001793107
Publikováno v:
Biochemistry. 47:12175-12184
We have studied the effects of lipid structure on the function of the mechanosensitive channel of large conductance (MscL) from Escherichia coli to determine whether effects follow from direct interaction between the lipids and protein or whether the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fd04200651d94a11198592345e3badf
https://doi.org/10.1021/bi801352a
https://doi.org/10.1021/bi801352a
Publikováno v:
Biochemistry. 47:4317-4328
The mechanosensitive channel of large conductance MscL from Escherichia coli has been reconstituted into sealed vesicles, and the effects of lipid structure on the flux of the fluorescent molecule calcein through the open channel have been studied. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::932317ab0aeda4f5d60cd91e582fbe6f
https://doi.org/10.1021/bi702409t
https://doi.org/10.1021/bi702409t
Autor:
Maurits R.R. de Planque, Andrew M. Powl, Alexander J. Henderson, Hywel Morgan, Bonnie A. Wallace, Shimul Chandra Saha
Publikováno v:
PLoS ONE
PLoS ONE, Vol 10, Iss 7, p e0131286 (2015)
PLoS ONE, Vol 10, Iss 7, p e0131286 (2015)
This paper describes the use of a newly-developed micro-chip bilayer platform to examine the electrophysiological properties of the prokaryotic voltage-gated sodium channel pore (Na(v)Sp) from Silicibacter pomeroyi. The platform allows up to 6 bilaye
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f530ec5b1d58ab01978fd6ebb9115f7
https://pubmed.ncbi.nlm.nih.gov/26147601
https://pubmed.ncbi.nlm.nih.gov/26147601
Publikováno v:
Biochemical Society Transactions. 33:905-909
Interactions between a membrane protein and the lipid molecules that surround it in the membrane are important in determining the structure and function of the protein. These interactions can be pictured at the molecular level using fluorescence spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6f1a5c2c90699ff28b2ffc4968a40dd
https://doi.org/10.1042/bst0330905
https://doi.org/10.1042/bst0330905
Publikováno v:
Biochemistry. 44:5713-5721
The hydrophobic thickness of a membrane protein is an important parameter, defining how the protein sits within the hydrocarbon core of the lipid bilayer that surrounds it in a membrane. Here we show that Trp scanning mutagenesis combined with fluore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7368120f7151282aa494798481811bd7
https://doi.org/10.1021/bi047338g
https://doi.org/10.1021/bi047338g